Structural Basis for Phosphotyrosine Recognition by Suppressor of Cytokine Signaling-3

Structure

Volumn 14, Issue 8, 2006, Pages 1285-1292

  Bergamin, Elisa ^a   Wu, Jinhua ^a   Hubbard, Stevan R ^a  

^a NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOKINE RECEPTOR; GLYCOPROTEIN GP 130; JANUS KINASE; PHOSPHOTYROSINE; PROTEIN SH2; SUPPRESSOR OF CYTOKINE SIGNALING 1; SUPPRESSOR OF CYTOKINE SIGNALING 3;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE INSERTION; MOLECULAR MECHANICS; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN TARGETING;

AMINO ACID SEQUENCE; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; CYTOKINE RECEPTOR GP130; JANUS KINASE 2; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHOSPHOTYROSINE; PROTEIN-TYROSINE KINASES; PROTO-ONCOGENE PROTEINS; SEQUENCE ALIGNMENT; SIGNAL TRANSDUCTION; SUPPRESSOR OF CYTOKINE SIGNALING PROTEINS;

EID: 33746860377     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2006.06.011     Document Type: Article

References (40)

1. Alexander W.S., and Hilton D.J. The role of suppressors of cytokine signaling (SOCS) proteins in regulation of the immune response. Annu. Rev. Immunol. 22 (2004) 503-529
2. Babon J.J., Yao S., DeSouza D.P., Harrison C.F., Fabri L.J., Liepinsh E., Scrofani S.D., Baca M., and Norton R.S. Secondary structure assignment of mouse SOCS3 by NMR defines the domain boundaries and identifies an unstructured insertion in the SH2 domain. FEBS J. 272 (2005) 6120-6130
3. Babon J.J., McManus E.J., Yao S., DeSouza D.P., Mielke L.A., Sprigg N.S., Willson T.A., Hilton D.J., Nicola N.A., Baca M., et al. The structure of SOCS3 reveals the basis of the extended SH2 domain function and identifies an unstructured insertion that regulates stability. Mol. Cell 22 (2006) 205-216
4. Betancourt M.R., and Skolnick J. Local propensities and statistical potentials of backbone dihedral angles in proteins. J. Mol. Biol. 342 (2004) 635-649
5. Bjorbak C., Lavery H.J., Bates S.H., Olson R.K., Davis S.M., Flier J.S., and Myers Jr. M.G. SOCS3 mediates feedback inhibition of the leptin receptor via Tyr985. J. Biol. Chem. 275 (2000) 40649-40657
6. Brünger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J.S., Kuszewski J., Nilges M., Pannu N.S., et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crytallogr. 54 (1998) 905-921
7. Bullock A.N., Debreczeni J.E., Edwards A.M., Sundstrom M., and Knapp S. Crystal structure of the SOCS2-elongin C-elongin B complex defines a prototypical SOCS box ubiquitin ligase. Proc. Natl. Acad. Sci. USA 103 (2006) 7637-7642
8. Croker B.A., Krebs D.L., Zhang J.G., Wormald S., Willson T.A., Stanley E.G., Robb L., Greenhalgh C.J., Forster I., Clausen B.E., et al. SOCS3 negatively regulates IL-6 signaling in vivo. Nat. Immunol. 4 (2003) 540-545
9. De Souza D., Fabri L.J., Nash A., Hilton D.J., Nicola N.A., and Baca M. SH2 domains from suppressor of cytokine signaling-3 and protein tyrosine phosphatase SHP-2 have similar binding specificities. Biochemistry 41 (2002) 9229-9236
10. Depetris R.S., Hu J., Gimpelevich I., Holt L.J., and Hubbard S.R. Structural basis for inhibition of the insulin receptor by the adaptor protein Grb14. Mol. Cell 20 (2005) 325-333
11. Eck M.J., Shoelson S.E., and Harrison S.C. Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck. Nature 362 (1993) 87-91
12. Emanuelli B., Peraldi P., Filloux C., Sawka-Verhelle D., Hilton D., and Van Obberghen E. SOCS-3 is an insulin-induced negative regulator of insulin signaling. J. Biol. Chem. 275 (2000) 15985-15991
13. Eyckerman S., Broekaert D., Verhee A., Vandekerckhove J., and Tavernier J. Identification of the Y985 and Y1077 motifs as SOCS3 recruitment sites in the murine leptin receptor. FEBS Lett. 486 (2000) 33-37
14. Hendrickson W.A. Transformations to optimize the superposition of similar structures. Acta Crystallogr. A 35 (1979) 158-163
15. Hilton D.J., Richardson R.T., Alexander W.S., Viney E.M., Willson T.A., Sprigg N.S., Starr R., Nicholson S.E., Metcalf D., and Nicola N.A. Twenty proteins containing a C-terminal SOCS box form five structural classes. Proc. Natl. Acad. Sci. USA 95 (1998) 114-119
16. Hof P., Pluskey S., Dhe-Paganon S., Eck M.J., and Shoelson S.E. Crystal structure of the tyrosine phosphatase SHP-2. Cell 92 (1998) 441-450
17. Hu J., and Hubbard S.R. Structural characterization of a novel Cbl phosphotyrosine recognition motif in the APS family of adapter proteins. J. Biol. Chem. 280 (2005) 18943-18949
18. Ihle J.N., and Kerr I.M. Jaks and Stats in signaling by the cytokine receptor superfamily. Trends Genet. 11 (1995) 69-74
19. Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47 (1991) 110-119
20. Kuriyan J., and Cowburn D. Modular peptide recognition domains in eukaryotic signaling. Annu. Rev. Biophys. Biomol. Struct. 26 (1997) 259-288
21. Lee C.H., Kominos D., Jacques S., Margolis B., Schlessinger J., Shoelson S.E., and Kuriyan J. Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase. Structure 2 (1994) 423-438
22. Li S.C., Gish G., Yang D., Coffey A.J., Forman-Kay J.D., Ernberg I., Kay L.E., and Pawson T. Novel mode of ligand binding by the SH2 domain of the human XLP disease gene product SAP/SH2D1A. Curr. Biol. 9 (1999) 1355-1362
23. Lucet I.S., Fantino E., Styles M., Bamert R., Patel O., Broughton S.E., Walter M., Burns C.J., Treutlein H., Wilks A.F., and Rossjohn J. The structural basis of Janus kinase 2 inhibition by a potent and specific pan-Janus kinase inhibitor. Blood 107 (2006) 176-183
24. Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr. 53 (1997) 240-255
25. Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50 (1994) 157-163
26. Nicholls A., Sharp K.A., and Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11 (1991) 281-296
27. Nicholson S.E., De Souza D., Fabri L.J., Corbin J., Willson T.A., Zhang J.G., Silva A., Asimakis M., Farley A., Nash A.D., et al. Suppressor of cytokine signaling-3 preferentially binds to the SHP-2-binding site on the shared cytokine receptor subunit gp130. Proc. Natl. Acad. Sci. USA 97 (2000) 6493-6498
28. Otwinowski Z. MLPHARE. In: Wolf W., Evans P.R., and Leslie A.G.W. (Eds). CCP4 Proceedings (1991), SERC Daresbury Laboratory, Warrington, UK 80-88
29. Otwinowski Z., and Minor W. Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
30. Poy F., Yaffe M.B., Sayos J., Saxena K., Morra M., Sumegi J., Cantley L.C., Terhorst C., and Eck M.J. Crystal structures of the XLP protein SAP reveal a class of SH2 domains with extended, phosphotyrosine-independent sequence recognition. Mol. Cell 4 (1999) 555-561
31. Roberts A.W., Robb L., Rakar S., Hartley L., Cluse L., Nicola N.A., Metcalf D., Hilton D.J., and Alexander W.S. Placental defects and embryonic lethality in mice lacking suppressor of cytokine signaling 3. Proc. Natl. Acad. Sci. USA 98 (2001) 9324-9329
32. Sasaki A., Yasukawa H., Suzuki A., Kamizono S., Syoda T., Kinjyo I., Sasaki M., Johnston J.A., and Yoshimura A. Cytokine-inducible SH2 protein-3 (CIS3/SOCS3) inhibits Janus tyrosine kinase by binding through the N-terminal kinase inhibitory region as well as SH2 domain. Genes Cells 4 (1999) 339-351
33. Sasaki A., Yasukawa H., Shouda T., Kitamura T., Dikic I., and Yoshimura A. CIS3/SOCS-3 suppresses erythropoietin (EPO) signaling by binding the EPO receptor and JAK2. J. Biol. Chem. 275 (2000) 29338-29347
34. Schmitz J., Weissenbach M., Haan S., Heinrich P.C., and Schaper F. SOCS3 exerts its inhibitory function on interleukin-6 signal transduction through the SHP2 recruitment site of gp130. J. Biol. Chem. 275 (2000) 12848-12856
35. Schwede T., Kopp J., Guex N., and Peitsch M.C. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31 (2003) 3381-3385
36. Takahashi Y., Carpino N., Cross J.C., Torres M., Parganas E., and Ihle J.N. SOCS3: an essential regulator of LIF receptor signaling in trophoblast giant cell differentiation. EMBO J. 22 (2003) 372-384
37. Terwilliger T.C., and Berendzen J. Automated MAD and MIR structure solution. Acta Crystallogr. D Biol. Crystallogr. 55 (1999) 849-861
38. Ueki K., Kondo T., and Kahn C.R. Suppressor of cytokine signaling 1 (SOCS-1) and SOCS-3 cause insulin resistance through inhibition of tyrosine phosphorylation of insulin receptor substrate proteins by discrete mechanisms. Mol. Cell. Biol. 24 (2004) 5434-5446
39. Waksman G., Shoelson S.E., Pant N., Cowburn D., and Kuriyan J. Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms. Cell 72 (1993) 779-790
40. Yasukawa H., Misawa H., Sakamoto H., Masuhara M., Sasaki A., Wakioka T., Ohtsuka S., Imaizumi T., Matsuda T., Ihle J.N., and Yoshimura A. The JAK-binding protein JAB inhibits Janus tyrosine kinase activity through binding in the activation loop. EMBO J. 18 (1999) 1309-1320